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Volumn 43, Issue 49, 2004, Pages 15550-15556

Effects of the antibiotic pulvomycin on the elongation factor Tu-dependent reactions. Comparison with other antibiotics

Author keywords

[No Author keywords available]

Indexed keywords

ADDITIVES; DISSOCIATION; POSITIVE IONS; PROTEINS; RNA; SYNTHESIS (CHEMICAL);

EID: 10644274430     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0487084     Document Type: Article
Times cited : (17)

References (29)
  • 3
    • 15844393667 scopus 로고    scopus 로고
    • Enacyloxin, an inhibitor of protein synthesis that acts on elongation factor Tu and the ribosome
    • Cetin, R., Anborgh, P. H., Cool, R. H., Watanabe, T., Sugiyama, T., Izaki, K., and Parmeggiani, A. (1996) Enacyloxin, an inhibitor of protein synthesis that acts on elongation factor Tu and the ribosome, EMBO J. 15, 2604-2611.
    • (1996) EMBO J. , vol.15 , pp. 2604-2611
    • Cetin, R.1    Anborgh, P.H.2    Cool, R.H.3    Watanabe, T.4    Sugiyama, T.5    Izaki, K.6    Parmeggiani, A.7
  • 4
    • 0033521195 scopus 로고    scopus 로고
    • Mutant EF-Tu species reveal novel features of the enacyloxin IIa inhibition on the ribosome
    • Zuurmond, A. M., Olsthoom-Tieleman, L. N., De Graaf, J. M, Parmeggiani, A., and Kraal, B. (1999) Mutant EF-Tu species reveal novel features of the enacyloxin IIa inhibition on the ribosome, J. Mol. Biol. 294, 627-637.
    • (1999) J. Mol. Biol. , vol.294 , pp. 627-637
    • Zuurmond, A.M.1    Olsthoom-Tieleman, L.N.2    De Graaf, J.M.3    Parmeggiani, A.4    Kraal, B.5
  • 5
    • 0026030903 scopus 로고
    • New antibiotic that acts specifically on the GTP-bound form of elongation factor Tu
    • Anborgh, P. H., and Parmeggiani, A. (1991) New antibiotic that acts specifically on the GTP-bound form of elongation factor Tu, EMBO J. 10, 779-784.
    • (1991) EMBO J. , vol.10 , pp. 779-784
    • Anborgh, P.H.1    Parmeggiani, A.2
  • 6
    • 0027362064 scopus 로고
    • Probing the reactivity of the GTP- and GDP-bound conformations of elongation factor Tu in complex with the antibiotic GE2270 A
    • Anborgh, P. H., and Parmeggiani, A. (1993) Probing the reactivity of the GTP- and GDP-bound conformations of elongation factor Tu in complex with the antibiotic GE2270 A, J. Biol. Chem. 268, 24622-24628.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24622-24628
    • Anborgh, P.H.1    Parmeggiani, A.2
  • 7
    • 0034635128 scopus 로고    scopus 로고
    • Structure of an EF-Tu complex with thiazolyl peptide antibiotic determined at 2.35 Å resolution: Atomic basis for GE2270 a inhibition of EF-Tu
    • Heffron, S. E., and Jurnak, F. (2000) Structure of an EF-Tu complex with thiazolyl peptide antibiotic determined at 2.35 Å resolution: atomic basis for GE2270 A inhibition of EF-Tu, Biochemistry 39, 37-45.
    • (2000) Biochemistry , vol.39 , pp. 37-45
    • Heffron, S.E.1    Jurnak, F.2
  • 8
    • 0035907234 scopus 로고    scopus 로고
    • Conformational changes of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu-GDP and aurodox
    • Vogeley, L., Palm, J. J., Mesters, J. R., and Hilgenfeld, R. (2001) Conformational changes of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu-GDP and aurodox, J. Biol. Chem. 276, 149-155.
    • (2001) J. Biol. Chem. , vol.276 , pp. 149-155
    • Vogeley, L.1    Palm, J.J.2    Mesters, J.R.3    Hilgenfeld, R.4
  • 10
    • 0026726745 scopus 로고
    • Site-directed mutagenesis of elongation factor Tu. The functional and structural role of residue Cys81
    • Anborgh, P. H., Parmeggiani, A., and Jonák, J. (1992) Site-directed mutagenesis of elongation factor Tu. The functional and structural role of residue Cys81, Eur. J. Biochem. 208, 251-257.
    • (1992) Eur. J. Biochem. , vol.208 , pp. 251-257
    • Anborgh, P.H.1    Parmeggiani, A.2    Jonák, J.3
  • 11
    • 0017847777 scopus 로고
    • Modification of the elongation factor Tu-guanine nucleotide interaction by kirromycin. A comparison with the effect of aminoacyl-tRNA and elongation factor Ts
    • Fasano, O., Bruns, W., Créchet, J.-B., Sander, G., and Parmeggiani, A. (1978) Modification of the elongation factor Tu-guanine nucleotide interaction by kirromycin. A comparison with the effect of aminoacyl-tRNA and elongation factor Ts, Eur. J. Biochem. 89, 557-565.
    • (1978) Eur. J. Biochem. , vol.89 , pp. 557-565
    • Fasano, O.1    Bruns, W.2    Créchet, J.-B.3    Sander, G.4    Parmeggiani, A.5
  • 12
    • 0019887609 scopus 로고
    • Modulation by monovalent and divalent cations of the guanosine-5′- triphosphatase activity dependent on elongation factor Tu
    • Ivell, R., Sander, G., and Parmeggiani, A. (1981) Modulation by monovalent and divalent cations of the guanosine-5′-triphosphatase activity dependent on elongation factor Tu, Biochemistry 20, 6852-6859.
    • (1981) Biochemistry , vol.20 , pp. 6852-6859
    • Ivell, R.1    Sander, G.2    Parmeggiani, A.3
  • 13
    • 0025640070 scopus 로고
    • The functional and structural roles of residues Gln114 and Glu117 in elongation factor Tu
    • Harmark, K., Cool, R. H., Clark, B. F. C., and Parmeggiani, A. (1990) The functional and structural roles of residues Gln114 and Glu117 in elongation factor Tu, Eur. J. Biochem. 194, 731-737.
    • (1990) Eur. J. Biochem. , vol.194 , pp. 731-737
    • Harmark, K.1    Cool, R.H.2    Clark, B.F.C.3    Parmeggiani, A.4
  • 14
    • 0013508244 scopus 로고
    • Pulvomycin, an inhibitor of protein biosynthesis preventing ternary complex formation between elongation factor Tu, GTP and aminoacyl-tRNA
    • Wolf, H., Assmann, D., and Fischer, E. (1978) Pulvomycin, an inhibitor of protein biosynthesis preventing ternary complex formation between elongation factor Tu, GTP and aminoacyl-tRNA, Proc. Natl. Acad. Sci. U.S.A. 75, 5324-5328.
    • (1978) Proc. Natl. Acad. Sci. U.S.A. , vol.75 , pp. 5324-5328
    • Wolf, H.1    Assmann, D.2    Fischer, E.3
  • 15
    • 0019964152 scopus 로고
    • The antibiotics kirromycin and pulvomycin bind to different sites in the elongation factor Tu from Escherichia coli
    • Pingoud, A., Block, W., Urbanke, C., and Wolf, H. (1982) The antibiotics kirromycin and pulvomycin bind to different sites in the elongation factor Tu from Escherichia coli, Eur. J. Biochem. 123, 261-265.
    • (1982) Eur. J. Biochem. , vol.123 , pp. 261-265
    • Pingoud, A.1    Block, W.2    Urbanke, C.3    Wolf, H.4
  • 16
    • 0031566186 scopus 로고    scopus 로고
    • Elongation factor Tu1 of the antibiotic GE2270A producer Planobispora rosea has an unexpected resistance profile against EF-Tu targeted antibiotics
    • Möhrle V. G., Tieleman L. N., and Kraal B. (1997) Elongation factor Tu1 of the antibiotic GE2270A producer Planobispora rosea has an unexpected resistance profile against EF-Tu targeted antibiotics, Biochem. Biophys. Res. Commun. 230, 320-326.
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 320-326
    • Möhrle, V.G.1    Tieleman, L.N.2    Kraal, B.3
  • 17
    • 0017581625 scopus 로고
    • Effect of kirromycin on elongation factor Tu. Location of the catalytic center for ribosome-elongation factor Tu GTPase activity on the elongation factor
    • Chinali, G., Wolf, H., and Parmeggiani, A. (1977) Effect of kirromycin on elongation factor Tu. Location of the catalytic center for ribosome-elongation factor Tu GTPase activity on the elongation factor, Eur. J. Biochem. 75, 55-65.
    • (1977) Eur. J. Biochem. , vol.75 , pp. 55-65
    • Chinali, G.1    Wolf, H.2    Parmeggiani, A.3
  • 18
    • 0032512429 scopus 로고    scopus 로고
    • Functional role of the noncatalytic domains of elongation factor Tu in the interaction with ligands
    • Cetin, R., Krab, I. M., Anborgh, P. H., Cool, R. H., and Parmeggiani, A. (1998) Functional role of the noncatalytic domains of elongation factor Tu in the interaction with ligands, Biochemistry 37, 486-495.
    • (1998) Biochemistry , vol.37 , pp. 486-495
    • Cetin, R.1    Krab, I.M.2    Anborgh, P.H.3    Cool, R.H.4    Parmeggiani, A.5
  • 19
    • 0020460281 scopus 로고
    • Preparation of nucleotide-free elongation factor Tu and its stabilization by the antibiotic kirromycin
    • Fasano, O., Crechet, J.-B., and Parmeggiani (1982) Preparation of nucleotide-free elongation factor Tu and its stabilization by the antibiotic kirromycin, Anal. Biochem. 124, 53-56.
    • (1982) Anal. Biochem. , vol.124 , pp. 53-56
    • Fasano, O.1    Crechet, J.-B.2    Parmeggiani3
  • 20
    • 0019430659 scopus 로고
    • Characterization of kirromycin-resistant elongation factor Tu from Escherichia coli
    • Ivell, R., Fasano, O., Crechet, J.-B., and Parmeggiani, A. (1981) Characterization of kirromycin-resistant elongation factor Tu from Escherichia coli, Biochemistry 20, 1355-1361.
    • (1981) Biochemistry , vol.20 , pp. 1355-1361
    • Ivell, R.1    Fasano, O.2    Crechet, J.-B.3    Parmeggiani, A.4
  • 21
    • 0018357476 scopus 로고
    • Conformational transition of protein synthesis elongation factor Tu induced by guanine nucleotides. Modulation by kirromycin and elongation factor Ts
    • Douglas, J., and Blumenthal, T. (1979) Conformational transition of protein synthesis elongation factor Tu induced by guanine nucleotides. Modulation by kirromycin and elongation factor Ts, J. Biol. Chem. 254, 5383-5387.
    • (1979) J. Biol. Chem. , vol.254 , pp. 5383-5387
    • Douglas, J.1    Blumenthal, T.2
  • 22
    • 0030025671 scopus 로고    scopus 로고
    • The structure of the Escherichia coli EF-Tu·EF-Ts complex at 2.5 a resolution
    • Kawashima, T., Berthet-Colominas, C., Wulff, M., Cusack, S., and Leberman, R. (1996) The structure of the Escherichia coli EF-Tu·EF-Ts complex at 2.5 A resolution, Nature 379, 511-518.
    • (1996) Nature , vol.379 , pp. 511-518
    • Kawashima, T.1    Berthet-Colominas, C.2    Wulff, M.3    Cusack, S.4    Leberman, R.5
  • 25
    • 0028836951 scopus 로고
    • Substitution of Arg230 and Arg233 in Escherichia coli Elongation factor Tu strongly enhances its pulvomycin resistance
    • Boon, K., Krab, I. M., Parmeggiani, A., Bosch, L., and Kraal, B. (1995) Substitution of Arg230 and Arg233 in Escherichia coli Elongation factor Tu strongly enhances its pulvomycin resistance, Eur. J. Biochem. 227, 816-822.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 816-822
    • Boon, K.1    Krab, I.M.2    Parmeggiani, A.3    Bosch, L.4    Kraal, B.5
  • 26
    • 0029835797 scopus 로고    scopus 로고
    • An elongation factor Tu (EF-Tu) resistant to the EF-Tu inhibitor GE2270 in the producing organism Planobispora rosea
    • Sosio, M., Amati, G., Cappellano, C., Sarubbi, E., Monti, F., and Donadio, S. (1996) An elongation factor Tu (EF-Tu) resistant to the EF-Tu inhibitor GE2270 in the producing organism Planobispora rosea, Mol. Microbiol. 22, 43-51.
    • (1996) Mol. Microbiol. , vol.22 , pp. 43-51
    • Sosio, M.1    Amati, G.2    Cappellano, C.3    Sarubbi, E.4    Monti, F.5    Donadio, S.6
  • 27
    • 0028913213 scopus 로고
    • Novel antibiotic, amythiamicins. IV. A mutation in the elongation factor Tu gene in a resistant mutant of B. subtilis
    • Shimanaka, K., Iinuma, H., Hamada, M., Ikeno, S., Tsuchiya, K. S., Arita, M., and Hori, M. (1995) Novel antibiotic, amythiamicins. IV. A mutation in the elongation factor Tu gene in a resistant mutant of B. subtilis, J. Antibiot. 48, 182-184
    • (1995) J. Antibiot. , vol.48 , pp. 182-184
    • Shimanaka, K.1    Iinuma, H.2    Hamada, M.3    Ikeno, S.4    Tsuchiya, K.S.5    Arita, M.6    Hori, M.7
  • 29
    • 0035943021 scopus 로고    scopus 로고
    • Elongation factor Ts can act as a steric chaperone by increasing the solubility of nucleotide binding-impaired elongation factor-Tu
    • Krab, I. M., te Biesebeke, R., Bernardi A, and Parmeggiani, A. (2001) Elongation factor Ts can act as a steric chaperone by increasing the solubility of nucleotide binding-impaired elongation factor-Tu, Biochemistry 40, 8531-8535.
    • (2001) Biochemistry , vol.40 , pp. 8531-8535
    • Krab, I.M.1    Te Biesebeke, R.2    Bernardi, A.3    Parmeggiani, A.4


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